Corticosteroid metabolism in human granulosa-lutein cells
OBJECTIVE The aims of this study were to determine the type and level of 11β‐hydroxysteroid dehydrogenase (11βHSD) in human granulosa‐leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing in vitro fertilization and embryo transfer...
Saved in:
Published in | Clinical endocrinology (Oxford) Vol. 48; no. 4; pp. 509 - 513 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford BSL
Blackwell Science Ltd, UK
01.04.1998
Blackwell |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | OBJECTIVE
The aims of this study were to determine the type and level of 11β‐hydroxysteroid dehydrogenase (11βHSD) in human granulosa‐leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing in vitro fertilization and embryo transfer (IVF/ET).
DESIGN
GLC from 32 patients undergoing IVF/ET were tested for type and level of 11βHSD activity in relation to treatment outcome.
PATIENTS
Periovulatory follicles were aspirated by ultrasound guided transvaginal puncture following a standard controlled ovarian stimulation protocol, ∼36 h after administering an ovulation‐inducing dose of human chorionic gonadotrophin (HCG). GLC were separated from follicular fluid by density‐gradient centrifugation and taken for measurement of 11βHSD activity in vitro; oocytes were used for IVF/ET.
MEASUREMENTS
Interconversion of cortisol (F) and cortisone (E), and dexamethasone (D) and 11‐dehydrodexamethasone (DHD) was measured in standardized assays comprising incubation of GLC with 3H‐labelled substrate, with separation of substrate and product by thin‐layer radiochromatography.
RESULTS
Conversion of F to E varied from 10.5 to 30.9% while that of E to F was between 2.4 and 44.6%. In the GLC of 25 patients in whom both activities were measured, dehydrogenase (F to E) activity predominated in 13 and reductase (E to F) in 12. By contrast, D (substrate for 11βHSD2 but not 11βHSD1) showed less than 1% metabolism in this system while DHD (substrate for 11βHSD1 and 11βHSD2) was converted significantly (65.6–90.5%) to D in the four patients tested. There was no significant difference in the interconversion of F and E between patients who became pregnant and those who did not.
CONCLUSIONS
The dehydrogenase and oxoreductase reactions catalysed by 11βHSD both occur in granulosa‐lutein cells at the time of follicular rupture, probably due to 11βHSD1. A lack of measurable conversion of dexamethasone to 11‐dehydrodexamethasone suggests that dehydrogenation due to 11βHSD2 is low or absent. Neither type nor level of 11βHSD activity measured under the present assay conditions correlates with IVF outcome. |
---|---|
AbstractList | OBJECTIVE
The aims of this study were to determine the type and level of 11β‐hydroxysteroid dehydrogenase (11βHSD) in human granulosa‐leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing
in vitro
fertilization and embryo transfer (IVF/ET).
DESIGN
GLC from 32 patients undergoing IVF/ET were tested for type and level of 11βHSD activity in relation to treatment outcome.
PATIENTS
Periovulatory follicles were aspirated by ultrasound guided transvaginal puncture following a standard controlled ovarian stimulation protocol, ∼36 h after administering an ovulation‐inducing dose of human chorionic gonadotrophin (HCG). GLC were separated from follicular fluid by density‐gradient centrifugation and taken for measurement of 11βHSD activity
in vitro
; oocytes were used for IVF/ET.
MEASUREMENTS
Interconversion of cortisol (F) and cortisone (E), and dexamethasone (D) and 11‐dehydrodexamethasone (DHD) was measured in standardized assays comprising incubation of GLC with
3
H‐labelled substrate, with separation of substrate and product by thin‐layer radiochromatography.
RESULTS
Conversion of F to E varied from 10.5 to 30.9% while that of E to F was between 2.4 and 44.6%. In the GLC of 25 patients in whom both activities were measured, dehydrogenase (F to E) activity predominated in 13 and reductase (E to F) in 12. By contrast, D (substrate for 11βHSD2 but not 11βHSD1) showed less than 1% metabolism in this system while DHD (substrate for 11βHSD1 and 11βHSD2) was converted significantly (65.6–90.5%) to D in the four patients tested. There was no significant difference in the interconversion of F and E between patients who became pregnant and those who did not.
CONCLUSIONS
The dehydrogenase and oxoreductase reactions catalysed by 11βHSD both occur in granulosa‐lutein cells at the time of follicular rupture, probably due to 11βHSD1. A lack of measurable conversion of dexamethasone to 11‐dehydrodexamethasone suggests that dehydrogenation due to 11βHSD2 is low or absent. Neither type nor level of 11βHSD activity measured under the present assay conditions correlates with IVF outcome. The aims of this study were to determine the type and level of 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) in human granulosa-leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing in vitro fertilization and embryo transfer (IVF/ET). GLC from 32 patients undergoing IVF/ET were tested for type and level of 11 beta HSD activity in relation to treatment outcome. Periovulatory follicles were aspirated by ultrasound guided transvaginal puncture following a standard controlled ovarian stimulation protocol, approximately 36 h after administering an ovulation-inducing dose of human chorionic gonadotrophin (HCG). GLC were separated from follicular fluid by density-gradient centrifugation and taken for measurement of 11 beta HSD activity in vitro; oocytes were used for IVF/ET. Interconversion of cortisol (F) and cortisone (E), and dexamethasone (D) and 11-dehydrodexamethasone (DHD) was measured in standardized assays comprising incubation of GLC with 3H-labelled substrate, with separation of substrate and product by thin-layer radiochromatography. Conversion of F to E varied from 10.5 to 30.9% while that of E to F was between 2.4 and 44.6%. In the GLC of 25 patients in whom both activities were measured, dehydrogenase (F to E) activity predominated in 13 and reductase (E to F) in 12. By contrast, D (substrate for 11 beta HSD2 but not 11 beta HSD1) showed less than 1% metabolism in this system while DHD (substrate for 11 beta HSD1 and 11 beta HSD2) was converted significantly (65.6-90.5%) to D in the four patients tested. There was no significant difference in the interconversion of F and E between patients who became pregnant and those who did not. The dehydrogenase and oxoreductase reactions catalysed by 11 beta HSD both occur in granulosa-lutein cells at the time of follicular rupture, probably due to 11 beta HSD1. A lack of measurable conversion of dexamethasone to 11-dehydrodexamethasone suggests that dehydrogenation due to 11 beta HSD2 is low or absent. Neither type nor level of 11 beta HSD activity measured under the present assay conditions correlates with IVF outcome. OBJECTIVEThe aims of this study were to determine the type and level of 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) in human granulosa-leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing in vitro fertilization and embryo transfer (IVF/ET). DESIGNGLC from 32 patients undergoing IVF/ET were tested for type and level of 11 beta HSD activity in relation to treatment outcome. PATIENTSPeriovulatory follicles were aspirated by ultrasound guided transvaginal puncture following a standard controlled ovarian stimulation protocol, approximately 36 h after administering an ovulation-inducing dose of human chorionic gonadotrophin (HCG). GLC were separated from follicular fluid by density-gradient centrifugation and taken for measurement of 11 beta HSD activity in vitro; oocytes were used for IVF/ET. MEASUREMENTSInterconversion of cortisol (F) and cortisone (E), and dexamethasone (D) and 11-dehydrodexamethasone (DHD) was measured in standardized assays comprising incubation of GLC with 3H-labelled substrate, with separation of substrate and product by thin-layer radiochromatography. RESULTSConversion of F to E varied from 10.5 to 30.9% while that of E to F was between 2.4 and 44.6%. In the GLC of 25 patients in whom both activities were measured, dehydrogenase (F to E) activity predominated in 13 and reductase (E to F) in 12. By contrast, D (substrate for 11 beta HSD2 but not 11 beta HSD1) showed less than 1% metabolism in this system while DHD (substrate for 11 beta HSD1 and 11 beta HSD2) was converted significantly (65.6-90.5%) to D in the four patients tested. There was no significant difference in the interconversion of F and E between patients who became pregnant and those who did not. CONCLUSIONSThe dehydrogenase and oxoreductase reactions catalysed by 11 beta HSD both occur in granulosa-lutein cells at the time of follicular rupture, probably due to 11 beta HSD1. A lack of measurable conversion of dexamethasone to 11-dehydrodexamethasone suggests that dehydrogenation due to 11 beta HSD2 is low or absent. Neither type nor level of 11 beta HSD activity measured under the present assay conditions correlates with IVF outcome. OBJECTIVE The aims of this study were to determine the type and level of 11β‐hydroxysteroid dehydrogenase (11βHSD) in human granulosa‐leutein cells (GLE) shortly before ovulation and to correlate activity with the outcome of treatment in patients undergoing in vitro fertilization and embryo transfer (IVF/ET). DESIGN GLC from 32 patients undergoing IVF/ET were tested for type and level of 11βHSD activity in relation to treatment outcome. PATIENTS Periovulatory follicles were aspirated by ultrasound guided transvaginal puncture following a standard controlled ovarian stimulation protocol, ∼36 h after administering an ovulation‐inducing dose of human chorionic gonadotrophin (HCG). GLC were separated from follicular fluid by density‐gradient centrifugation and taken for measurement of 11βHSD activity in vitro; oocytes were used for IVF/ET. MEASUREMENTS Interconversion of cortisol (F) and cortisone (E), and dexamethasone (D) and 11‐dehydrodexamethasone (DHD) was measured in standardized assays comprising incubation of GLC with 3H‐labelled substrate, with separation of substrate and product by thin‐layer radiochromatography. RESULTS Conversion of F to E varied from 10.5 to 30.9% while that of E to F was between 2.4 and 44.6%. In the GLC of 25 patients in whom both activities were measured, dehydrogenase (F to E) activity predominated in 13 and reductase (E to F) in 12. By contrast, D (substrate for 11βHSD2 but not 11βHSD1) showed less than 1% metabolism in this system while DHD (substrate for 11βHSD1 and 11βHSD2) was converted significantly (65.6–90.5%) to D in the four patients tested. There was no significant difference in the interconversion of F and E between patients who became pregnant and those who did not. CONCLUSIONS The dehydrogenase and oxoreductase reactions catalysed by 11βHSD both occur in granulosa‐lutein cells at the time of follicular rupture, probably due to 11βHSD1. A lack of measurable conversion of dexamethasone to 11‐dehydrodexamethasone suggests that dehydrogenation due to 11βHSD2 is low or absent. Neither type nor level of 11βHSD activity measured under the present assay conditions correlates with IVF outcome. |
Author | Thomas Mason Tetsuka Hillier |
Author_xml | – sequence: 1 givenname: F. J surname: THOMAS fullname: THOMAS, F. J organization: Department of Obstetrics and Gynaecology, University of Edinburgh Centre for Reproductive Biology, 37 Chalmers Street, Edinburgh, United Kingdom – sequence: 2 givenname: M. J surname: THOMAS fullname: THOMAS, M. J organization: Department of Obstetrics and Gynaecology, University of Edinburgh Centre for Reproductive Biology, 37 Chalmers Street, Edinburgh, United Kingdom – sequence: 3 givenname: M surname: TETSUKA fullname: TETSUKA, M organization: Department of Obstetrics and Gynaecology, University of Edinburgh Centre for Reproductive Biology, 37 Chalmers Street, Edinburgh, United Kingdom – sequence: 4 givenname: J. I surname: MASON fullname: MASON, J. I organization: Department of Clinical Biochemistry, University of Edinburgh Centre for Reproductive Biology, 37 Chalmers Street, Edinburgh, United Kingdom – sequence: 5 givenname: S. G surname: HILLIER fullname: HILLIER, S. G organization: Department of Obstetrics and Gynaecology, University of Edinburgh Centre for Reproductive Biology, 37 Chalmers Street, Edinburgh, United Kingdom |
BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2253194$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/9640419$$D View this record in MEDLINE/PubMed |
BookMark | eNqNkUtv1DAUhS1UVKYtPwEpC8Qu6fUjfkhsYChtpapopCLYWY7jgIckbu1ETP89DjOadVe-8jnH997PZ-hkDKNDqMBQYWD8clthyuuSEF5XWClZAbBaVLtXaHUUTtAKKEAJnLM36CylLQDUEsQpOlWcAcNqhdQ6xMnbkCYXg2-LwU2mCb1PQ-HH4vc8mLH4Fc049yGZsp8nl6-t6_t0gV53pk_u7eE8R9-_Xj2sb8q7b9e36093pWWKi1I2RAA03IpOSecItU3XdAoTcI4ZpVrSCA6UNmAUdlzhVgoqsLOdFLIVNT1HH_bvPsbwNLs06cGnZQIzujAnLVReRjKZjXJvtDGkFF2nH6MfTHzWGPRCTW_1AkcvcPRCTf-npnc5-u7QY24G1x6DB0xZf3_QTbKm7zIQ69PRRkhNsWLZ9nFv--t79_zi9np9dZ-LHC_3cZ9_Y3eMm_hH88yk1j_ur_VPvCGbL583Gug_EwOYYA |
CODEN | CLECAP |
CitedBy_id | crossref_primary_10_1034_j_1600_0897_2002_1o122_x crossref_primary_10_1016_j_fertnstert_2014_09_034 crossref_primary_10_1016_S0165_0378_98_00011_4 crossref_primary_10_1093_humupd_dmn021 crossref_primary_10_1095_biolreprod_106_053470 crossref_primary_10_1210_er_2003_0031 crossref_primary_10_1517_13543784_17_4_481 crossref_primary_10_1093_humrep_14_6_1563 crossref_primary_10_1016_j_apjr_2016_04_007 crossref_primary_10_1016_S0015_0282_99_00607_X crossref_primary_10_1016_S1472_6483_10_62091_3 crossref_primary_10_1053_beem_2000_0119 crossref_primary_10_3390_ijms13045138 crossref_primary_10_1017_S1751731117003755 crossref_primary_10_1095_biolreprod60_2_330 crossref_primary_10_1530_REP_15_0363 crossref_primary_10_1016_j_theriogenology_2019_03_007 crossref_primary_10_1016_j_fertnstert_2014_11_015 crossref_primary_10_1046_j_1365_2265_1999_00892_x crossref_primary_10_1111_j_1740_0929_2007_00414_x crossref_primary_10_1210_jc_2015_3899 crossref_primary_10_1530_rep_1_00272 crossref_primary_10_1097_00060793_199906000_00004 |
Cites_doi | 10.1016/0960-0760(92)90220-D 10.1210/jc.79.2.480 10.1016/S0015-0282(16)57798-X 10.1016/0140-6736(93)91710-4 10.1210/en.138.3.1305 10.1016/0303-7207(94)90176-7 10.1016/0303-7207(94)90279-8 10.1677/joe.0.1480419 10.1210/jc.82.5.1598 10.1016/0039-128X(94)00024-7 10.1093/oxfordjournals.humrep.a135740 10.1016/0303-7207(92)90064-D 10.1016/S0303-7207(97)00118-4 10.1111/j.1365-2265.1994.tb02438.x 10.1677/joe.0.1530041 10.1210/en.138.7.2948 |
ContentType | Journal Article |
Copyright | Blackwell Science Ltd, Oxford 1998 INIST-CNRS |
Copyright_xml | – notice: Blackwell Science Ltd, Oxford – notice: 1998 INIST-CNRS |
DBID | BSCLL IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1046/j.1365-2265.1998.00457.x |
DatabaseName | Istex Pascal-Francis Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | CrossRef MEDLINE MEDLINE - Academic |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine |
EISSN | 1365-2265 |
EndPage | 513 |
ExternalDocumentID | 10_1046_j_1365_2265_1998_00457_x 9640419 2253194 CEN457 ark_67375_WNG_X1Q2QDBQ_0 |
Genre | article Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- .3N .55 .GA .GJ .Y3 05W 08P 0R~ 10A 1OB 1OC 29B 31~ 33P 36B 3O- 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52R 52S 52T 52U 52V 52W 52X 53G 5GY 5HH 5LA 5RE 5VS 66C 6J9 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A01 A03 AAESR AAEVG AAHHS AAJUZ AAKAS AANLZ AAONW AAQQT AASGY AAVGM AAXRX AAZKR ABCQN ABCUV ABCVL ABEML ABHUG ABJNI ABPTK ABPVW ABQWH ABXGK ACAHQ ACBWZ ACCFJ ACCZN ACGFO ACGFS ACGOF ACMXC ACPOU ACPRK ACSCC ACXBN ACXME ACXQS ADAWD ADBBV ADBTR ADDAD ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZCM ADZMN ADZOD AEEZP AEGXH AEIGN AEIMD AENEX AEQDE AEQTP AEUQT AEUYR AFBPY AFEBI AFFNX AFFPM AFGKR AFPWT AFVGU AFZJQ AGJLS AHBTC AHEFC AHMBA AIACR AIAGR AIURR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMXJE BROTX BRXPI BSCLL BY8 C45 CAG COF CS3 D-6 D-7 D-E D-F DCZOG DPXWK DR2 DRFUL DRMAN DRSTM DU5 DUUFO EBS EJD EMOBN ESX EX3 F00 F01 F04 F5P FEDTE FUBAC FZ0 G-S G.N GODZA H.X HF~ HVGLF HZI HZ~ IHE IX1 J0M J5H K48 KBYEO LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MJL MK4 MRFUL MRMAN MRSTM MSFUL MSMAN MSSTM MXFUL MXMAN MXSTM N04 N05 N9A NF~ O66 O9- OVD P2P P2W P2X P2Z P4B P4D PALCI PQQKQ Q.N Q11 QB0 R.K REN RIWAO RJQFR ROL RX1 SAMSI SUPJJ TEORI UB1 V8K W8V W99 WBKPD WHWMO WIH WIJ WIK WOHZO WOW WQJ WRC WUP WVDHM WXI WXSBR X7M XG1 YOC YUY ZA5 ZGI ZXP ZZTAW ~IA ~WT AITYG HGLYW OIG 08R AAPBV AAUGY AKALU IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
ID | FETCH-LOGICAL-c4967-8b2700b6c7f98ee23cbfbf9120ee4a99d2b76033b0a91e691d87371ecf878d753 |
IEDL.DBID | DR2 |
ISSN | 0300-0664 |
IngestDate | Fri Aug 16 02:05:08 EDT 2024 Fri Aug 23 01:14:31 EDT 2024 Thu May 23 23:58:57 EDT 2024 Sun Oct 29 17:07:03 EDT 2023 Sat Aug 24 01:14:56 EDT 2024 Wed Jan 17 05:08:47 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 4 |
Keywords | Human Corticosteroid Enzyme Assisted procreation Lutein Exploration Metabolism Ovulation In vitro fertilization embryo transfer Enzymatic activity 11β-Hydroxysteroid dehydrogenase Female Oxidoreductases Granulosa Ovarian follicle |
Language | English |
License | CC BY 4.0 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4967-8b2700b6c7f98ee23cbfbf9120ee4a99d2b76033b0a91e691d87371ecf878d753 |
Notes | ark:/67375/WNG-X1Q2QDBQ-0 ArticleID:CEN457 istex:D33FBD45C58392698203B69E6682454F3B30AD7E ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 9640419 |
PQID | 79964848 |
PQPubID | 23479 |
PageCount | 5 |
ParticipantIDs | proquest_miscellaneous_79964848 crossref_primary_10_1046_j_1365_2265_1998_00457_x pubmed_primary_9640419 pascalfrancis_primary_2253194 wiley_primary_10_1046_j_1365_2265_1998_00457_x_CEN457 istex_primary_ark_67375_WNG_X1Q2QDBQ_0 |
PublicationCentury | 1900 |
PublicationDate | April 1998 |
PublicationDateYYYYMMDD | 1998-04-01 |
PublicationDate_xml | – month: 04 year: 1998 text: April 1998 |
PublicationDecade | 1990 |
PublicationPlace | Oxford BSL |
PublicationPlace_xml | – name: Oxford BSL – name: Oxford – name: England |
PublicationTitle | Clinical endocrinology (Oxford) |
PublicationTitleAlternate | Clinical Endocrinology |
PublicationYear | 1998 |
Publisher | Blackwell Science Ltd, UK Blackwell |
Publisher_xml | – name: Blackwell Science Ltd, UK – name: Blackwell |
References | Michael, A.E., Gregory, L., Thaventhiran, L., Antoniw, J.W., Cooke, B.A. (1996) Follicular variation in ovarian 11β-hydroxysteroid dehydrogenase (11βHSD) activities: evidence for the paracrine inhibition of 11βHSD in human granulosa-lutein cells. Journal of Endocrinology, 148, 419 425. Clarke, R.J., Thaventhiram, L., Michael, A.E., Antoniw, J.W., Cooke, B.A. (1995) Possible physiological significance of the inhibition of 11β-hydroxysteroid dehydrogenase (11βHSD) by progesterone and other ovarian steroids in human granulosa-lutein cells. Journal of Endocrinology, 147 (suppl.), 95. Michael, A.E., Evagelatou, M., Norgate, D.P., Clarke, R.J., Antoniw, J.W., Stedman, B.A., Brennan, A., Welsby, R., Bujalska, I., Stewart, P.M., Cooke, B.A. (1997) Isoforms of 11β-hydroxysteroid dehydrogenase in human granulosa-lutein cells. Molecular and Cellular Endocrinology, 132, 43 52. Krozowski, Z.S. (1992) 11β-hydroxysteroid dehydrogenase and the short-chain alcohol dehydrogenase (SCAD) superfamily. Molecular and Cellular Endocrinology, 84, C25 C31. Best, R., Nelson, S.M., Walker, B.R. (1997) Dexamethasone and 11-dehydrodexamethasone as tools to investigate the isozymes of 11β-hydroxysteroid dehydrogenase in vitro and in vivo. Journal of Endocrinology, 153, 41 48. Hillier, S.G. (1994) Cortisol and oocyte quality. Clinical Endocrinology, 40, 19 20. Michael, A.E. & Cooke, B.A. (1994) A working hypothesis for the regulation of steroidogenesis and germ cell development in the gonads by glucocorticoids and 11β-hydroxysteroid dehydrogenase (11βHSD). Molecular and Cellular Endocrinology, 100, 55 63. Li, K.X.Z., Obeyesekere, V.R., Krozowski, Z.S., Ferrari, P. (1997) Oxoreductase and dehydrogenase activities of the human and rat 11β-hydroxysteroid dehydrogenase type 2 enzyme. Endocrinology, 138, 2948 2952. Shimojo, M., Ricketts, M.L., Petrelli, M.D., Moradi, P., Johnson, P.D., Bradwell, A.R., Hewison, M., Howie, A.J., Stewart, P.M. (1997) Immunodetection of 11β-hydroxysteroid dehydrogenase type 2 in human mineralocorticoid target tissues: evidence for nuclear localization. Endocrinology, 138, 1305 1311. Albiston, A., Obeyesekere, V.R., Smith, R.E., Krozowski, Z.S. (1994) Cloning and tissue distribution of human 11beta-hydroxysteroid dehydrogenase type 2 enzyme. Molecular and Cellular Endcrinology, 105, R11 R17. Michael, A.E., Gregory, L., Piercy, E.C., Walker, S.M., Shaw, R.W., Cooke, B.A. (1995) Ovarian 11β-hydroxysteroid dehydrogenase activity is inversely related to the outcome of in vitro fertilization-embryo transfer treatment cycles . Fertility and Sterility, 64, 590 598. Stewart, P.M., Murry, B.A., Mason, J.I. (1994) Human kidney 11β-hydroxysteroid dehydrogenase is a high affinity nicotinamide adenine dinucleotide-dependent enzyme and differs from the cloned type 1 isoform. Journal of Clinical Endocrinology and Metabolism, 79, 480 484. Michael, A.E., Gregory, L., Walker, S.M., Antoniw, J.W., Shaw, R.W., Edwards, C.W.R., Cooke, B.A. (1993) Ovarian 11β-hydroxysteroid dehydrogenase: potential predictor of conception by in-vitro fertilisation and embryo transfer. Lancet, 342, 711 712. Stewart, P.M. & Mason, J.I. (1995) Cortisol to cortisone: glucocorticoid to mineralocorticoid. Steroids, 60, 143 146. Out, H.J., Mannaerts, B.M.J.L., Driessen, S.G.A.J., Coelingh Bennink, H.J.T. (1995) A prospective, randomized, assessor blind, multicentre study comparing recombinant and urinary follicle-stimulating hormone (Puregon vs. Metrodin) in in vitro fertilization. Human Reproduction, 10, 2534 2540. Tetsuka, M., Thomas, F.J., Thomas, M.J., Anderson, R.A., Mason, J.I., Hillier, S.G. (1997) Differential expression of messenger ribonucleic acids encoding 11β-hydroxysteroid dehydrogenase types 1 and 2 in human granulosa cells. Journal of Clinical Endocrinology and Metabolism, 82, 2006 2009. Diederich, S., Hanke, B., Oelkers, W., Bahr, V. (1997) Metabolism of dexamethasone in the human kidney: nicotinamide adenine dinucleotide-dependent 11beta-reduction. Journal of Clinical Endocrinology and Metabolism, 82, 1598 1602. Whorwood, C.B., Franklyn, J.A., Sheppard, M.C., Stewart, P.M. (1992) Tissue localization of 11β-hydroxysteroid dehydrogenase and its relationship to the glucocorticoid receptor. Journal of Steroid Biochemistry and Molecular Biology, 41, 21 28. 1995; 64 1997; 138 1994; 100 1994; 105 1995; 60 1997; 82 1997; 153 1997; 132 1995; 10 1994; 79 1995; 147 1996; 148 1994; 40 1992; 84 1993; 342 1992; 41 Clarke R.J. (e_1_2_6_4_2) 1995; 147 e_1_2_6_8_2 e_1_2_6_7_2 e_1_2_6_9_2 e_1_2_6_19_2 Tetsuka M. (e_1_2_6_18_2) 1997; 82 e_1_2_6_3_2 e_1_2_6_6_2 e_1_2_6_5_2 e_1_2_6_12_2 e_1_2_6_13_2 e_1_2_6_2_2 e_1_2_6_10_2 e_1_2_6_11_2 e_1_2_6_16_2 e_1_2_6_17_2 e_1_2_6_14_2 e_1_2_6_15_2 |
References_xml | – volume: 148, start-page: 419 year: 1996 end-page: 425 article-title: Follicular variation in ovarian 11β‐hydroxysteroid dehydrogenase (11βHSD) activities: evidence for the paracrine inhibition of 11βHSD in human granulosa‐lutein cells publication-title: Journal of Endocrinology – volume: 105, start-page: R11 year: 1994 end-page: R17 article-title: Cloning and tissue distribution of human 11beta‐hydroxysteroid dehydrogenase type 2 enzyme publication-title: Molecular and Cellular Endcrinology – volume: 40, start-page: 19 year: 1994 end-page: 20 article-title: Cortisol and oocyte quality publication-title: Clinical Endocrinology – volume: 82, start-page: 2006 year: 1997 end-page: 2009 article-title: Differential expression of messenger ribonucleic acids encoding 11β‐hydroxysteroid dehydrogenase types 1 and 2 in human granulosa cells publication-title: Journal of Clinical Endocrinology and Metabolism – volume: 41, start-page: 21 year: 1992 end-page: 28 article-title: Tissue localization of 11β‐hydroxysteroid dehydrogenase and its relationship to the glucocorticoid receptor publication-title: Journal of Steroid Biochemistry and Molecular Biology – volume: 64, start-page: 590 year: 1995 end-page: 598 article-title: Ovarian 11β‐hydroxysteroid dehydrogenase activity is inversely related to the outcome of fertilization–embryo transfer treatment cycles publication-title: Fertility and Sterility – volume: 82, start-page: 1598 year: 1997 end-page: 1602 article-title: Metabolism of dexamethasone in the human kidney: nicotinamide adenine dinucleotide‐dependent 11beta‐reduction publication-title: Journal of Clinical Endocrinology and Metabolism – volume: 138, start-page: 2948 year: 1997 end-page: 2952 article-title: Oxoreductase and dehydrogenase activities of the human and rat 11β‐hydroxysteroid dehydrogenase type 2 enzyme publication-title: Endocrinology – volume: 342, start-page: 711 year: 1993 end-page: 712 article-title: Ovarian 11β‐hydroxysteroid dehydrogenase: potential predictor of conception by fertilisation and embryo transfer publication-title: Lancet – volume: 84, start-page: C25 year: 1992 end-page: C31 article-title: 11β‐hydroxysteroid dehydrogenase and the short‐chain alcohol dehydrogenase (SCAD) superfamily publication-title: Molecular and Cellular Endocrinology – volume: 147 start-page: 95 issue: suppl. year: 1995 article-title: Possible physiological significance of the inhibition of 11β‐hydroxysteroid dehydrogenase (11βHSD) by progesterone and other ovarian steroids in human granulosa‐lutein cells publication-title: Journal of Endocrinology – volume: 79, start-page: 480 year: 1994 end-page: 484 article-title: Human kidney 11β‐hydroxysteroid dehydrogenase is a high affinity nicotinamide adenine dinucleotide‐dependent enzyme and differs from the cloned type 1 isoform publication-title: Journal of Clinical Endocrinology and Metabolism – volume: 60, start-page: 143 year: 1995 end-page: 146 article-title: Cortisol to cortisone: glucocorticoid to mineralocorticoid publication-title: Steroids – volume: 10, start-page: 2534 year: 1995 end-page: 2540 article-title: A prospective, randomized, assessor blind, multicentre study comparing recombinant and urinary follicle‐stimulating hormone (Puregon vs. Metrodin) in fertilization publication-title: Human Reproduction – volume: 100, start-page: 55 year: 1994 end-page: 63 article-title: A working hypothesis for the regulation of steroidogenesis and germ cell development in the gonads by glucocorticoids and 11β‐hydroxysteroid dehydrogenase (11βHSD) publication-title: Molecular and Cellular Endocrinology – volume: 132, start-page: 43 year: 1997 end-page: 52 article-title: Isoforms of 11β‐hydroxysteroid dehydrogenase in human granulosa‐lutein cells publication-title: Molecular and Cellular Endocrinology – volume: 138, start-page: 1305 year: 1997 end-page: 1311 article-title: Immunodetection of 11β‐hydroxysteroid dehydrogenase type 2 in human mineralocorticoid target tissues: evidence for nuclear localization publication-title: Endocrinology – volume: 153, start-page: 41 year: 1997 end-page: 48 article-title: Dexamethasone and 11‐dehydrodexamethasone as tools to investigate the isozymes of 11β‐hydroxysteroid dehydrogenase and publication-title: Journal of Endocrinology – ident: e_1_2_6_19_2 doi: 10.1016/0960-0760(92)90220-D – ident: e_1_2_6_17_2 doi: 10.1210/jc.79.2.480 – ident: e_1_2_6_11_2 doi: 10.1016/S0015-0282(16)57798-X – ident: e_1_2_6_12_2 doi: 10.1016/0140-6736(93)91710-4 – ident: e_1_2_6_15_2 doi: 10.1210/en.138.3.1305 – ident: e_1_2_6_2_2 doi: 10.1016/0303-7207(94)90176-7 – ident: e_1_2_6_9_2 doi: 10.1016/0303-7207(94)90279-8 – ident: e_1_2_6_13_2 doi: 10.1677/joe.0.1480419 – ident: e_1_2_6_5_2 doi: 10.1210/jc.82.5.1598 – ident: e_1_2_6_16_2 doi: 10.1016/0039-128X(94)00024-7 – ident: e_1_2_6_14_2 doi: 10.1093/oxfordjournals.humrep.a135740 – ident: e_1_2_6_7_2 doi: 10.1016/0303-7207(92)90064-D – ident: e_1_2_6_10_2 doi: 10.1016/S0303-7207(97)00118-4 – volume: 147 start-page: 95 year: 1995 ident: e_1_2_6_4_2 article-title: Possible physiological significance of the inhibition of 11β‐hydroxysteroid dehydrogenase (11βHSD) by progesterone and other ovarian steroids in human granulosa‐lutein cells publication-title: Journal of Endocrinology contributor: fullname: Clarke R.J. – ident: e_1_2_6_6_2 doi: 10.1111/j.1365-2265.1994.tb02438.x – volume: 82 start-page: 2006 year: 1997 ident: e_1_2_6_18_2 article-title: Differential expression of messenger ribonucleic acids encoding 11β‐hydroxysteroid dehydrogenase types 1 and 2 in human granulosa cells publication-title: Journal of Clinical Endocrinology and Metabolism contributor: fullname: Tetsuka M. – ident: e_1_2_6_3_2 doi: 10.1677/joe.0.1530041 – ident: e_1_2_6_8_2 doi: 10.1210/en.138.7.2948 |
SSID | ssj0005807 |
Score | 1.7307228 |
Snippet | OBJECTIVE
The aims of this study were to determine the type and level of 11β‐hydroxysteroid dehydrogenase (11βHSD) in human granulosa‐leutein cells (GLE)... The aims of this study were to determine the type and level of 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) in human granulosa-leutein cells (GLE)... OBJECTIVEThe aims of this study were to determine the type and level of 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) in human granulosa-leutein cells... |
SourceID | proquest crossref pubmed pascalfrancis wiley istex |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 509 |
SubjectTerms | 11-beta-Hydroxysteroid Dehydrogenases Biological and medical sciences Birth control Cells, Cultured Chorionic Gonadotropin - therapeutic use Cortisone - metabolism Dexamethasone - metabolism Embryo Transfer Female Fertilization in Vitro Follicular Phase - physiology Granulosa Cells - enzymology Gynecology. Andrology. Obstetrics Humans Hydrocortisone - metabolism Hydroxysteroid Dehydrogenases - metabolism Luteal Cells - enzymology Medical sciences Sterility. Assisted procreation Treatment Outcome |
Title | Corticosteroid metabolism in human granulosa-lutein cells |
URI | https://api.istex.fr/ark:/67375/WNG-X1Q2QDBQ-0/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1046%2Fj.1365-2265.1998.00457.x https://www.ncbi.nlm.nih.gov/pubmed/9640419 https://search.proquest.com/docview/79964848 |
Volume | 48 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3NatwwEBYlgdJL_0PdNq0PpTcvlixLFj2l26ShkIUtDd2bkCypLJvYZb0Loac-Qp8xT5IZ2btlSw6l9GKMxRjrG81o5Pkj5I0RZeGMtxlcRcZd7jLrDcuMDZWqQx585PTZRJye80-zcjbEP2EuTF8fYvvDDSUj6msUcGP7LiR5rG67idBiosSUOwyJ5KUcoT2JdfXQPvr8u5JUOWROF5hILQQfgnoGB-etL9rZqfYR9CuMnDQdgBf6rhe3maW7Vm7cpk4ekMVmgn10ymK0XtlR_eOP2o__B4GH5P5gzaZH_fJ7RO745jG5ezb465-Qd-MWhzCRZNnOXXrpV7DoLubdZTpv0tgfMP0Gk1xftJ25_vkLxMDDAHoTuqfk_OT4y_g0G9o1ZDVXoG4ri05sK2oZVOU9K2obbFCU5d5zo5RjVoq8KGxuFPVCUVfJQlJfh0pWDo5NB2SvaRv_DFgjAqspY5bSwAXj1lLpnCvg_OTBwDAJoRvW6O99VQ4dvekcM88QFY2oaERFR1T0VULeRh5uCcxygVFtstRfJx_1jE7Z9MP7qc4TcrjD5C0BqD5QWDwhrzdM1yCLCIlpfLvutITDI694lZCDfi1sSeF5zqlKSBkZ-tcfrcfHE7h5_o90L8i9PocSI41ekr3Vcu0PwYha2VdRPG4Ak68Orw |
link.rule.ids | 315,786,790,1382,27957,27958,46329,46753 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Pb9MwFLfQJgEX_k8LbCwHxC0ldhwn0U6jbBRYKxVtojfLjm1UrUtQ00rTTnwEPuM-yd5z0qKiHRDiEkWxXhS_n9_Ls98_Qt4okSZGWR3BVUTcxCbSVrFIaZcXpYud9UgPR2Jwzj9P0knXDghzYdr6EOsDN5QMr69RwPFA-l3nlmyl3IdoMZFizh3GRPI064FBuQ3Sn_r91dfftaTSLnc6wVRqIXgX1tO5OO9808a_ahvZfoWxk6oB9rm278Vdhummnet_VCePyWw1xTY-5aK3XOheef1H9cf_xIMn5FFn0IZH7Qp8Su7Z6hm5P-xc9s_JYb_GIcwlmddTE17aBay72bS5DKdV6FsEht9hlstZ3aibn79AEiwMoEOheUHOT47P-oOo69gQlbwAjZtr9GNrUWauyK1lSamddgVlsbVcFYVhOhNxkuhYFdSKgpo8SzJqS5dnuQHMdshWVVd2F7ARjpWUMU2p44JxrWlmjElgC2XBxlABoSts5I-2MIf0DnWOyWfIFYlckcgV6bkirwLy1oO4JlDzCwxsy1L5bfRRTuiYjT-8H8s4IPsbKK8JQPuBzuIBOVihLkEckSWqsvWykRnsH3nO84DstIthTQrPY06LgKQe0b_-aNk_HsHNy3-kOyAPBmfDU3n6afTlFXnYplRi4NEe2VrMl3YfbKqFfu1l5RaZ7hLR |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQK1VcoDwqAi3NAXHLEjuOk6gnutulPLpiERV7s-zYRqttk2qzK1U98RP6G_klzDjZRYt6QIhLFMWaKJ6Xx5lvxoS8UiJNjLI6gquIuIlNpK1ikdIuL0oXO-slfTYSp-f8wySddPgnrIVp-0Osf7ihZXh_jQZ-ZdybLivZGrlHaDGRYskdQiJ5mvUgntzmImGo4YMvv1tJpV3pdIKV1ELwDtXTZTjvfNPGUrWNXL9G6KRqgHuuPfbirrh0M8z169TwIZmtZtjCU2a95UL3yps_mj_-HxbskgddOBu-bfXvEblnq8dk56xL2D8hR_0ah7CSZF5PTXhpF6B1F9PmMpxWoT8gMPwOk1xe1I36-eMW7MDCAKYTmqfkfHjytX8adec1RCUvwN_mGrPYWpSZK3JrWVJqp11BWWwtV0VhmM5EnCQ6VgW1oqAmz5KM2tLlWW5g37RHtqq6ss9ANMKxkjKmKXVcMK41zYwxCWygLEQYKiB0JRp51bblkD6dzrH0DLkikSsSuSI9V-R1QF57Ga4J1HyGsLYsld9G7-SEjtl4cDyWcUAONoS8JgDfBx6LB-RwJXQJxogsUZWtl43MYPfIc54HZK_VhTUpPI85LQKSeoH-9UfL_skIbp7_I90h2fk8GMpP70cfX5D7bT0loo72ydZivrQHEFAt9EtvKb8ARnMRgA |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Corticosteroid+metabolism+in+human+granulosa-lutein+cells&rft.jtitle=Clinical+endocrinology+%28Oxford%29&rft.au=Thomas%2C+F+J&rft.au=Thomas%2C+M+J&rft.au=Tetsuka%2C+M&rft.au=Mason%2C+J+I&rft.date=1998-04-01&rft.issn=0300-0664&rft.volume=48&rft.issue=4&rft.spage=509&rft.epage=513&rft_id=info:doi/10.1046%2Fj.1365-2265.1998.00457.x&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0300-0664&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0300-0664&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0300-0664&client=summon |